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B5R760 (B5R760_SALG2) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase HAMAP-Rule MF_00834
EC=2.6.1.62 HAMAP-Rule MF_00834
Alternative name(s):
7,8-diamino-pelargonic acid aminotransferase HAMAP-Rule MF_00834
7,8-diaminononanoate synthase HAMAP-Rule MF_00834
Diaminopelargonic acid synthase HAMAP-Rule MF_00834
Gene names
Name:bioA HAMAP-Rule MF_00834
Ordered Locus Names:SG0771
OrganismSalmonella gallinarum (strain 287/91 / NCTC 13346) [Complete proteome] [HAMAP] EMBL CAR36667.1
Taxonomic identifier550538 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor By similarity. HAMAP-Rule MF_00834

Catalytic activity

S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate. HAMAP-Rule MF_00834

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00834

Pathway

Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. HAMAP-Rule MF_00834

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00834

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00834.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. HAMAP-Rule MF_00834

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region112 – 1132Pyridoxal phosphate binding By similarity HAMAP-Rule MF_00834
Region308 – 3092Pyridoxal phosphate binding By similarity HAMAP-Rule MF_00834

Sites

Binding site521Substrate By similarity HAMAP-Rule MF_00834
Binding site1441Substrate By similarity HAMAP-Rule MF_00834
Binding site2451Pyridoxal phosphate By similarity HAMAP-Rule MF_00834
Binding site2741Substrate By similarity HAMAP-Rule MF_00834
Binding site3071Substrate; via carbonyl oxygen By similarity HAMAP-Rule MF_00834
Binding site3911Substrate By similarity HAMAP-Rule MF_00834
Site171Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM By similarity HAMAP-Rule MF_00834

Amino acid modifications

Modified residue2741N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00834

Sequences

Sequence LengthMass (Da)Tools
B5R760 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: 53569D13CD6B6156

FASTA42947,303
        10         20         30         40         50         60 
MTTDDLAFDK RHIWHPYTSM TSPLPVYPVE RAEGCELVLA SGERLIEGMS SWWAAIHGYN 

        70         80         90        100        110        120 
HPQLNAAMKA QIDAMSHVMF GGITHTPAVN LCRKLVAITP EPLECVFLAD SGSVSVEVAM 

       130        140        150        160        170        180 
KMALQYWQAR GESRQRFLTF RHGYHGDTFG AMSVCDPDNS MHSLWKGYLP ENLFAPAPQS 

       190        200        210        220        230        240 
RMDGEWDESD IAPFARLMAA HRHEIAAVIL EPIVQGAGGM RIYHPQWLRR IRNMCDREGI 

       250        260        270        280        290        300 
LLIADEIATG FGRTGKLFAC EHAGIAPDIL CLGKALTGGT MTLSATLTTR QVAETISNGE 

       310        320        330        340        350        360 
AGCFMHGPTF MGNPLACAVA CASLTLLESG EWRQQVASIE SQLRAELAPA QSSPWVADVR 

       370        380        390        400        410        420 
VLGAIGVVET THTVNMAALQ RFFVGQGVWI RPFGKLIYLM PPYIIRPDQL RRLTQAVNDA 


VHNETFFSH

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References

[1]"Comparative genome analysis of Salmonella Enteritidis PT4 and Salmonella Gallinarum 287/91 provides insights into evolutionary and host adaptation pathways."
Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. expand/collapse author list , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Sanders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphrey T., Roberts M., Barrow P.A., Dougan G., Parkhill J.
Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 287/91 / NCTC 13346.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM933173 Genomic DNA. Translation: CAR36667.1.
RefSeqYP_002225853.1. NC_011274.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING550538.SG0771.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR36667; CAR36667; SG0771.
GeneID6925336.
KEGGseg:SG0771.
PATRIC18499779. VBISalEnt1629_0831.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020209.
KOK00833.
OMADRVFYAD.
ProtClustDBPRK07986.

Enzyme and pathway databases

BioCycSENT550538:GJ93-775-MONOMER.
UniPathwayUPA00078; UER00160.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00834. BioA.
InterProIPR005814. Aminotrans_3.
IPR005815. BioA.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF8. PTHR11986:SF8. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00508. bioA. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB5R760_SALG2
AccessionPrimary (citable) accession number: B5R760
Entry history
Integrated into UniProtKB/TrEMBL: November 4, 2008
Last sequence update: November 4, 2008
Last modified: May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info